ID   CATA_BRUSU              Reviewed;         499 AA.
AC   Q8FWU0;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 42.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=BRA0355;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; AE014292; AAN33553.1; -; Genomic_DNA.
DR   RefSeq; NP_699548.1; -.
DR   HSSP; P42321; 1M85.
DR   GeneID; 1164793; -.
DR   GenomeReviews; AE014292_GR; BRA0355.
DR   KEGG; bms:BRA0355; -.
DR   NMPDR; fig|204722.1.peg.2457; -.
DR   TIGR; BRA0355; -.
DR   HOGENOM; Q8FWU0; -.
DR   BioCyc; BSUI204722:BR_A0355-MON; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR011614; Catalase_N.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; FALSE_NEG.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Periplasm; Peroxidase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    499       Catalase.
FT                                /FTId=PRO_0000084982.
FT   ACT_SITE     55     55       By similarity.
FT   ACT_SITE    127    127       By similarity.
FT   METAL       337    337       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   499 AA;  56462 MW;  8ADC6CA375A31A48 CRC64;
     MTDRPIMTTS AGAPIPDNQN SLTAGERGPI LMQDYQLIEK LSHQNRERIP ERAVHAKGWG
     AYGTLTITGD ISRYTKAKVL QPGAQTPMLA RFSTVAGELG AADAERDVRG FALKFYTQEG
     NWDLVGNNTP VFFVRDPLKF PDFIHTQKRH PRTHLRSATA MWDFWSLSPE SLHQVTILMS
     DRGLPTDVRH INGYGSHTYS FWNDAGERYW VKFHFKTMQG HKHWTNAEAE QVIGRTREST
     QEDLFSAIEN GEFPKWKVQV QIMPELDADK TPYNPFDLTK VWPHADYPPI DIGVMELNRN
     PENYFTEVEN AAFSPSNIVP GIGFSPDKML QARIFSYADA HRHRLGTHYE SIPVNQPKCL
     VHHYHRDGQM NVYGGIKTGN PDAYYEPNSF NGPVEQPSAK EPPLCISGNA DRYNHRIGND
     DYSQPRALFN LFDAAQKQRL FSNIAAAMKG VPGFIVERQL GHFKLIHPEY EAGVRKALKD
     AHGYDANTIA LNEKITAAE
//